(data stored in ACNUC8465 zone)

SWISSPROT: Q6FJE7_CANGA

ID   Q6FJE7_CANGA            Unreviewed;       248 AA.
AC   Q6FJE7;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   10-APR-2019, entry version 64.
DE   RecName: Full=Protein-lysine N-methyltransferase EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03198};
DE   AltName: Full=Elongation factor methyltransferase 6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN   Name=EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN   OrderedLocusNames=CAGL0M06897g {ECO:0000313|CGD:CAL0137099,
GN   ECO:0000313|EMBL:CAG62623.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62623.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that methylates elongation factor 1-alpha.
CC       {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. METTL21 family. EFM6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03198}.
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DR   EMBL; CR380959; CAG62623.1; -; Genomic_DNA.
DR   RefSeq; XP_449647.1; XM_449647.1.
DR   STRING; 5478.XP_449647.1; -.
DR   EnsemblFungi; CAG62623; CAG62623; CAGL0M06897g.
DR   GeneID; 2891696; -.
DR   KEGG; cgr:CAGL0M06897g; -.
DR   CGD; CAL0137099; CAGL0M06897g.
DR   EuPathDB; FungiDB:CAGL0M06897g; -.
DR   eggNOG; ENOG410ISZC; Eukaryota.
DR   eggNOG; ENOG4111PIY; LUCA.
DR   HOGENOM; HOG000187553; -.
DR   InParanoid; Q6FJE7; -.
DR   KO; K21804; -.
DR   OMA; HILYIRK; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03198; Methyltr_EFM6; 1.
DR   InterPro; IPR033684; EFM6.
DR   InterPro; IPR019410; Methyltransf_16.
DR   Pfam; PF10294; Methyltransf_16; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJE7.
DR   SWISS-2DPAGE; Q6FJE7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   REGION       88     90       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING      50     50       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
FT   BINDING     116    116       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING     144    144       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
FT   BINDING     171    171       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03198}.
SQ   SEQUENCE   248 AA;  28000 MW;  FF198D3BFD72B023 CRC64;
     MEDILGFGDL IESRPVEHMG QSDLTFNGML VPGLKIYEDG GESGCGGKVW IAGELLCEFI
     LEKSRDGELL KDWINDDSVS FGNVLELGSG TGLVGLCVGL VTKKQSQRMV KTYITDIDQL
     VPLMEKNVEL NLIDQQVFAK ELLWGEALPI EFAPVKTGHA TTSSLDLVLA ADCVYLEKAF
     PLLEKTLLDL TECDNPPVIL MAYRKRRKAD KHFFQKIRKN FNVIVINDFK NYDQYLKQRT
     HLFQLVRK
//

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